Hemin inhibits transfer of pre-δ-aminolevulinate synthase into chick embryo liver mitochondria
Autor: | Brian K. May, Gopesh Srivastava, J.D. Brooker, John C. Wallace, Iain A. Borthwick, W.H. Elliott |
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Rok vydání: | 1983 |
Předmět: |
Pulse labelling
Biophysics Mitochondria Liver Chick Embryo Heme Mitochondrion Biochemistry chemistry.chemical_compound Cytosol polycyclic compounds Animals heterocyclic compounds Molecular Biology Pyruvate Carboxylase Enzyme Precursors ATP synthase biology Embryo Cell Biology equipment and supplies δ aminolevulinate synthase Pyruvate carboxylase Molecular Weight Liver chemistry biology.protein Protein Processing Post-Translational 5-Aminolevulinate Synthetase Hemin |
Zdroj: | Biochemical and Biophysical Research Communications. 117:344-349 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(83)91582-6 |
Popis: | Pulse labelling studies in chick embryo livers show that hemin prevents the transfer of drug induced pre-δ-aminolevulinate synthase from the cytosol into the mitochondria, leading to an accumulation of precursor in the cytosol. No effect of hemin was observed on the transfer of pre-pyruvate carboxylase into mitochondria. These results eliminated a general toxic effect of hemin on mitochondrial import of proteins and are consistent with the view that hemin specifically inhibits the transfer of ALA synthase. |
Databáze: | OpenAIRE |
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